ID   GNTK_BACLI              Reviewed;         513 AA.
AC   P46834;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1995, sequence version 1.
DT   03-AUG-2022, entry version 84.
DE   RecName: Full=Gluconokinase;
DE            EC=2.7.1.12;
DE   AltName: Full=Gluconate kinase;
GN   Name=gntK;
OS   Bacillus licheniformis.
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX   NCBI_TaxID=1402;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=BGSC5A2;
RX   PubMed=8535972; DOI=10.1093/dnares/1.4.157;
RA   Yoshida K., Seki S., Fujita Y.;
RT   "Nucleotide sequence and features of the Bacillus licheniformis gnt
RT   operon.";
RL   DNA Res. 1:157-162(1994).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + D-gluconate = 6-phospho-D-gluconate + ADP + H(+);
CC         Xref=Rhea:RHEA:19433, ChEBI:CHEBI:15378, ChEBI:CHEBI:18391,
CC         ChEBI:CHEBI:30616, ChEBI:CHEBI:58759, ChEBI:CHEBI:456216;
CC         EC=2.7.1.12;
CC   -!- ACTIVITY REGULATION: Catabolite repression by gluconate.
CC   -!- PATHWAY: Carbohydrate acid metabolism; D-gluconate degradation.
CC   -!- SIMILARITY: Belongs to the FGGY kinase family. {ECO:0000305}.
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DR   EMBL; D31631; BAA06502.1; -; Genomic_DNA.
DR   PIR; JC2304; JC2304.
DR   AlphaFoldDB; P46834; -.
DR   SMR; P46834; -.
DR   UniPathway; UPA00792; -.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0046316; F:gluconokinase activity; IEA:UniProtKB-EC.
DR   GO; GO:0046177; P:D-gluconate catabolic process; IEA:UniProtKB-UniPathway.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   InterPro; IPR043129; ATPase_NBD.
DR   InterPro; IPR000577; Carb_kinase_FGGY.
DR   InterPro; IPR018485; Carb_kinase_FGGY_C.
DR   InterPro; IPR018483; Carb_kinase_FGGY_CS.
DR   InterPro; IPR018484; Carb_kinase_FGGY_N.
DR   InterPro; IPR006002; Gluconate_kinase.
DR   Pfam; PF02782; FGGY_C; 1.
DR   Pfam; PF00370; FGGY_N; 1.
DR   PIRSF; PIRSF000538; GlpK; 1.
DR   SUPFAM; SSF53067; SSF53067; 2.
DR   TIGRFAMs; TIGR01314; gntK_FGGY; 1.
DR   PROSITE; PS00933; FGGY_KINASES_1; 1.
DR   PROSITE; PS00445; FGGY_KINASES_2; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Gluconate utilization; Kinase; Nucleotide-binding;
KW   Transferase.
FT   CHAIN           1..513
FT                   /note="Gluconokinase"
FT                   /id="PRO_0000059543"
FT   BINDING         16
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
FT   BINDING         261
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
FT   BINDING         300
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
FT   BINDING         412..416
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   513 AA;  56804 MW;  99AFBD42602ECFA8 CRC64;
     MTSYMLGIDI GTTSTKAVLF SEKGDVIQKE SIGYALYTPD ISTAEQNPDE IFQAVIQSTA
     KIMQQHPDKQ PSFISFSSAM HSVIAMDEND KPLTSCITWA DNRSEGWAHK IKEEMNGHNV
     YKRTGTPIHP MAPLSKITWI VNEHPEIAVK AKKYIGIKEY IFKKLFDQYV VDYSLASAMG
     MMNLKTLAWD EEALAIAGIT PDHLSKLVPT TAIFHHCNPE LAAMMGIDPQ TPFVIGASDG
     VLSNLGVNAI KKGEIAVTIG TSGAIRPIID KPQTDEKGRI FCYALTENHW VIGGPVNNGG
     IVLRWIRDEF ASSEIETAKR LGIDPYDVLT KIAERVRPGA DGLLFHPYLA GERAPLWNPD
     VPGSFFGLTM SHKKEHMIRA ALEGVIYNLY TVFLALTECM DGPVARIQAT GGFARSDVWR
     QMMADIFESE VVVPESYESS CLGACILGLY ATGKIDSFDV VSDMIGSTHR HAPKEESAKE
     YRKLMPLFIN LSRALENEYT QIANYQRSLS SKK